3V1R
Crystal structures of the reverse transcriptase-associated ribonuclease H domain of XMRV with inhibitor beta-thujaplicinol
Summary for 3V1R
| Entry DOI | 10.2210/pdb3v1r/pdb |
| Related | 3V1O 3V1Q |
| Descriptor | Reverse transcriptase/ribonuclease H p80, SULFATE ION, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (6 entities in total) |
| Functional Keywords | reverse transcription, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Xenotropic MuLV-related virus VP35 (XMRV) |
| Cellular location | Gag-Pol polyprotein: Host cell membrane; Lipid-anchor (Potential). Matrix protein p15: Virion (Potential). Capsid protein p30: Virion (Potential). Nucleocapsid protein p10: Virion (Potential): Q2F7J3 |
| Total number of polymer chains | 1 |
| Total formula weight | 20666.97 |
| Authors | Zhou, D.,Wlodawer, A. (deposition date: 2011-12-09, release date: 2012-03-14, Last modification date: 2024-02-28) |
| Primary citation | Zhou, D.,Chung, S.,Miller, M.,Le Grice, S.F.,Wlodawer, A. Crystal structures of the reverse transcriptase-associated ribonuclease H domain of xenotropic murine leukemia-virus related virus. J.Struct.Biol., 177:638-645, 2012 Cited by PubMed Abstract: The ribonuclease H (RNase H) domain of retroviral reverse transcriptase (RT) plays a critical role in the life cycle by degrading the RNA strands of DNA/RNA hybrids. In addition, RNase H activity is required to precisely remove the RNA primers from nascent (-) and (+) strand DNA. We report here three crystal structures of the RNase H domain of xenotropic murine leukemia virus-related virus (XMRV) RT, namely (i) the previously identified construct from which helix C was deleted, (ii) the intact domain, and (iii) the intact domain complexed with an active site α-hydroxytropolone inhibitor. Enzymatic assays showed that the intact RNase H domain retained catalytic activity, whereas the variant lacking helix C was only marginally active, corroborating the importance of this helix for enzymatic activity. Modeling of the enzyme-substrate complex elucidated the essential role of helix C in binding a DNA/RNA hybrid and its likely mode of recognition. The crystal structure of the RNase H domain complexed with β-thujaplicinol clearly showed that coordination by two divalent cations mediates recognition of the inhibitor. PubMed: 22366278DOI: 10.1016/j.jsb.2012.02.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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